Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structural plasticity and catalysis regulation of a thermosensor histidine kinase.

Proceedings of the National Academy of Sciences of the United States of America - 22 Sept 2009

Albanesi Daniela, Martín Mariana, Trajtenberg Felipe, Mansilla María C, Haouz Ahmed, Alzari Pedro M, de Mendoza Diego, Buschiazzo Alejandro

Abstract excerpt

Temperature sensing is essential for the survival of living cells. A major challenge is to understand how a biological thermometer processes thermal information to optimize cellular functions. Using structural and biochemical approaches, we show that the thermosensitive histidine kinase, DesK, from Bacillus subtilis is cold-activated through specific interhelical rearrangements in its central four-helix bundle...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Adenosine Triphosphate
Share to Bacillus subtilis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Catalysis

Share to Chromatography, Gel

Share to Crystallization

Share to Crystallography, X-Ray

Share to Histidine Kinase

Share to Protein Kinases

Source

Open in PubMed Open full text

Identifiers

PMID: 19805278
DOI: 10.1073/pnas.0906699106
PMCID: PMC2738621

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural plasticity and catalysis regulation of a thermosensor histidine kinase.PMID 19805278Read ↗

A Transmembrane Histidine Kinase Functions as a pH Sensor.Semantic proximity Read ↗

Structure of the entire cytoplasmic portion of a sensor histidine-kinase protein.Semantic proximity Read ↗

Revisiting the pH-gated conformational switch on the activities of HisKA-family histidine kinases.Semantic proximity Read ↗

Structural insights into the signal transduction mechanism of the K+-sensing two-component system KdpDE.Semantic proximity Read ↗

A pH-gated conformational switch regulates the phosphatase activity of bifunctional HisKA-family histidine kinases.Semantic proximity Read ↗

Helix bundle loops determine whether histidine kinases autophosphorylate in cis or in trans.Semantic proximity Read ↗

Switching Protein Conformational Substates by Protonation and Mutation.Semantic proximity Read ↗

A Trigger Residue for Transmembrane Signaling in the Escherichia coli Serine Chemoreceptor.Semantic proximity Read ↗

Structure and binding specificity of the receiver domain of sensor histidine kinase CKI1 from Arabidopsis thaliana.Semantic proximity Read ↗

An unorthodox sensory adaptation site in the Escherichia coli serine chemoreceptor.Semantic proximity Read ↗

The HAMP domain structure implies helix rotation in transmembrane signaling.Semantic proximity Read ↗

Stability and binding of the phosphorylated species of the N-terminal domain of enzyme I and the histidine phosphocarrier protein from the Streptomyces coelicolor phosphoenolpyruvate:sugar phosphotransferase system.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.